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Database: PDB
Entry: 3LN6
LinkDB: 3LN6
Original site: 3LN6 
HEADER    LIGASE                                  02-FEB-10   3LN6              
TITLE     CRYSTAL STRUCTURE OF A BIFUNCTIONAL GLUTATHIONE SYNTHETASE FROM       
TITLE    2 STREPTOCOCCUS AGALACTIAE                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE BIOSYNTHESIS BIFUNCTIONAL PROTEIN GSHAB;       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: GAMMA-GCS-GS, GCS-GS, GLUTAMATE-CYSTEINE LIGASE, GAMMA-     
COMPND   5 GLUTAMYLCYSTEINE SYNTHETASE, GAMMA-ECS, GCS, GLUTATHIONE SYNTHETASE, 
COMPND   6 GLUTATHIONE SYNTHASE, GSH SYNTHETASE, GSH-S, GSHASE, GS;             
COMPND   7 EC: 6.3.2.2, 6.3.2.3;                                                
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS AGALACTIAE SEROGROUP V;           
SOURCE   3 ORGANISM_TAXID: 216466;                                              
SOURCE   4 STRAIN: BAA-811;                                                     
SOURCE   5 GENE: GSHAB, GSHF, SAG1821;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET11A                                    
KEYWDS    GAMMA-GLUTAMYL CYSTEINE LIGASE DOMAIN, ATP-GRASP DOMAIN, HYBRID       
KEYWDS   2 ENZYME, ATP-BINDING, GLUTATHIONE BIOSYNTHESIS, LIGASE, MAGNESIUM,    
KEYWDS   3 MANGANESE, METAL-BINDING, MULTIFUNCTIONAL ENZYME, NUCLEOTIDE-BINDING 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.STOUT,B.VERGAUWEN,S.N.SAVVIDES                                      
REVDAT   1   13-APR-11 3LN6    0                                                
JRNL        AUTH   J.STOUT,D.DE VOS,B.VERGAUWEN,S.N.SAVVIDES                    
JRNL        TITL   STRUCTURES OF TWO BIFUNCTIONAL GAMMA-GLUTAMATE-CYSTEINE      
JRNL        TITL 2 LIGASE/GLUTATHIONE SYNTHETASES (GSHF) REVEAL A NOVEL HYBRID  
JRNL        TITL 3 ATP-GRASP FOLD                                               
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 23309                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.253                           
REMARK   3   FREE R VALUE                     : 0.286                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1178                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1  4.6700 -  4.0800    0.01        0   145  0.2070 0.2600        
REMARK   3     2  4.0800 -  3.7100    0.01        0   148  0.2470 0.3160        
REMARK   3     3  3.7100 -  3.4500    0.01        0   142  0.2740 0.2730        
REMARK   3     4  3.4500 -  3.2500    0.01        0   142  0.3000 0.3550        
REMARK   3     5  3.2500 -  3.0800    0.01        0   145  0.3220 0.4180        
REMARK   3     6  3.0800 -  2.9500    0.01        0   153  0.3530 0.4280        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 76.73                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 95.45                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.03000                                             
REMARK   3    B22 (A**2) : -1.03000                                             
REMARK   3    B33 (A**2) : 2.07000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.014           NULL                                  
REMARK   3   ANGLE     :  1.512           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: MLHL MAXIMUM LIKELIHOOD REFINEMENT        
REMARK   3  PROCEDURE                                                           
REMARK   4                                                                      
REMARK   4 3LN6 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-FEB-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB057484.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-FEB-07; 12-JUL-08               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG; ESRF           
REMARK 200  BEAMLINE                       : BW7A; ID14-2                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0720; 0.9330                     
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM; ADSC QUANTUM 210R  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24531                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 8.400                              
REMARK 200  R MERGE                    (I) : 0.07700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.13200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS, MR                    
REMARK 200 SOFTWARE USED: SOLVE, MOLREP, PHASER                                 
REMARK 200 STARTING MODEL: 1V4G, 1UC8                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.97                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M (NH4)2SO4, 100MM TRIS-HCL PH 8.5,   
REMARK 280  12% GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   -X+1/2,Y,-Z+3/4                                         
REMARK 290       6555   X,-Y+1/2,-Z+1/4                                         
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X,-Y,Z                                                 
REMARK 290      11555   -Y+1/2,X,Z+3/4                                          
REMARK 290      12555   Y,-X+1/2,Z+1/4                                          
REMARK 290      13555   -X,Y+1/2,-Z+1/4                                         
REMARK 290      14555   X+1/2,-Y,-Z+3/4                                         
REMARK 290      15555   Y,X,-Z                                                  
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       71.51000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       71.51000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      105.61500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       71.51000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       52.80750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       71.51000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      158.42250            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       71.51000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      158.42250            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       71.51000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       52.80750            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000       71.51000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       71.51000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      105.61500            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       71.51000            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       71.51000            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      105.61500            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       71.51000            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      158.42250            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       71.51000            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       52.80750            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       71.51000            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       52.80750            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       71.51000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      158.42250            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       71.51000            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       71.51000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      105.61500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 61850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      143.02000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 785  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ILE A     2                                                      
REMARK 465     ILE A     3                                                      
REMARK 465     LEU A   250                                                      
REMARK 465     ILE A   251                                                      
REMARK 465     SER A   314                                                      
REMARK 465     SER A   315                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A   9    CD   NE   CZ   NH1  NH2                             
REMARK 470     HIS A  13    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ILE A  16    CD1                                                 
REMARK 470     ILE A  30    CD1                                                 
REMARK 470     GLN A  35    CG   CD   OE1  NE2                                  
REMARK 470     ARG A  36    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A  37    CG1  CG2                                            
REMARK 470     THR A  40    OG1  CG2                                            
REMARK 470     LYS A  44    CG   CD   CE   NZ                                   
REMARK 470     TYR A  59    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE A  67    CD1                                                 
REMARK 470     ILE A  70    CD1                                                 
REMARK 470     VAL A 107    CG1  CG2                                            
REMARK 470     ARG A 108    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A 109    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 110    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 111    CG   OD1  OD2                                       
REMARK 470     ILE A 112    CD1                                                 
REMARK 470     ILE A 114    CG1  CG2  CD1                                       
REMARK 470     LEU A 117    CG   CD1  CD2                                       
REMARK 470     PHE A 121    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 122    CG   CD   OE1  OE2                                  
REMARK 470     TYR A 123    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP A 124    CG   OD1  OD2                                       
REMARK 470     TYR A 125    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A 126    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 127    CG   CD   CE   NZ                                   
REMARK 470     TYR A 128    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 130    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 131    CG   CD   CE   NZ                                   
REMARK 470     THR A 132    OG1  CG2                                            
REMARK 470     LYS A 135    CG   CD   CE   NZ                                   
REMARK 470     LEU A 136    CG   CD1  CD2                                       
REMARK 470     ILE A 137    CD1                                                 
REMARK 470     ILE A 140    CD1                                                 
REMARK 470     GLU A 152    CD   OE1  OE2                                       
REMARK 470     LEU A 160    CG   CD1  CD2                                       
REMARK 470     ILE A 167    CD1                                                 
REMARK 470     ASP A 168    CG   OD1  OD2                                       
REMARK 470     LYS A 176    CD   CE   NZ                                        
REMARK 470     ARG A 183    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A 202    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP A 204    CG   OD1  OD2                                       
REMARK 470     GLN A 205    CD   OE1  NE2                                       
REMARK 470     LYS A 206    CG   CD   CE   NZ                                   
REMARK 470     LEU A 207    CG   CD1  CD2                                       
REMARK 470     VAL A 211    CG1  CG2                                            
REMARK 470     LEU A 214    CG   CD1  CD2                                       
REMARK 470     SER A 217    OG                                                  
REMARK 470     VAL A 222    CG1  CG2                                            
REMARK 470     ASN A 223    CG   OD1                                            
REMARK 470     HIS A 224    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 225    CG   CD   CE   NZ                                   
REMARK 470     ASP A 226    CG   OD1  OD2                                       
REMARK 470     ILE A 227    CD1                                                 
REMARK 470     ARG A 228    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 229    CD1                                                 
REMARK 470     SER A 230    OG                                                  
REMARK 470     TYR A 231    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 234    CG   CD1  CD2                                       
REMARK 470     LYS A 235    CG   CD   CE   NZ                                   
REMARK 470     VAL A 238    CG1  CG2                                            
REMARK 470     ASN A 239    CG   OD1                                            
REMARK 470     LEU A 241    CG   CD1  CD2                                       
REMARK 470     ASN A 243    CG   OD1                                            
REMARK 470     LYS A 246    CE   NZ                                             
REMARK 470     SER A 247    OG                                                  
REMARK 470     GLU A 253    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 254    CG   CD   CE   NZ                                   
REMARK 470     GLU A 255    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 261    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A 269    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 270    CG   OD1                                            
REMARK 470     TYR A 271    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 272    CG   CD1  CD2                                       
REMARK 470     GLU A 273    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 274    CG   CD   CE   NZ                                   
REMARK 470     ILE A 276    CD1                                                 
REMARK 470     ILE A 292    CD1                                                 
REMARK 470     LEU A 304    CG   CD1  CD2                                       
REMARK 470     ILE A 312    CG1  CG2  CD1                                       
REMARK 470     ASP A 313    CG   OD1  OD2                                       
REMARK 470     SER A 316    OG                                                  
REMARK 470     ILE A 318    CG1  CG2  CD1                                       
REMARK 470     ASP A 319    CG   OD1  OD2                                       
REMARK 470     GLN A 320    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 321    CG   OD1  OD2                                       
REMARK 470     ILE A 322    CG1  CG2  CD1                                       
REMARK 470     LYS A 323    CG   CD   CE   NZ                                   
REMARK 470     GLU A 324    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 327    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 331    CG   CD1  CD2                                       
REMARK 470     ILE A 332    CG1  CG2  CD1                                       
REMARK 470     SER A 335    OG                                                  
REMARK 470     LEU A 338    CG   CD1  CD2                                       
REMARK 470     GLU A 339    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 341    CG   CD1  CD2                                       
REMARK 470     GLN A 359    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 362    CG   OD1                                            
REMARK 470     SER A 364    OG                                                  
REMARK 470     ARG A 376    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 378    CG1  CG2  CD1                                       
REMARK 470     GLU A 382    CG   CD   OE1  OE2                                  
REMARK 470     MET A 392    SD   CE                                             
REMARK 470     ILE A 393    CD1                                                 
REMARK 470     LEU A 396    CG   CD1  CD2                                       
REMARK 470     LYS A 440    CD   CE   NZ                                        
REMARK 470     VAL A 446    CG1  CG2                                            
REMARK 470     GLN A 450    CD   OE1  NE2                                       
REMARK 470     SER A 460    OG                                                  
REMARK 470     ILE A 462    CD1                                                 
REMARK 470     LYS A 473    CD   CE   NZ                                        
REMARK 470     ILE A 477    CD1                                                 
REMARK 470     LYS A 485    CG   CD   CE   NZ                                   
REMARK 470     ILE A 491    CG1  CG2  CD1                                       
REMARK 470     PHE A 505    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP A 507    CG   OD1  OD2                                       
REMARK 470     ARG A 508    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 509    CE   NZ                                             
REMARK 470     ASN A 513    CG   OD1                                            
REMARK 470     PHE A 515    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     GLN A 517    CD   OE1  NE2                                       
REMARK 470     ILE A 518    CG1  CG2  CD1                                       
REMARK 470     GLN A 519    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 521    NZ                                                  
REMARK 470     ILE A 523    CD1                                                 
REMARK 470     LYS A 526    CE   NZ                                             
REMARK 470     LYS A 528    CG   CD   CE   NZ                                   
REMARK 470     SER A 529    OG                                                  
REMARK 470     THR A 530    OG1  CG2                                            
REMARK 470     ASN A 531    CG   OD1                                            
REMARK 470     LEU A 534    CG   CD1  CD2                                       
REMARK 470     ILE A 536    CG1  CG2  CD1                                       
REMARK 470     ILE A 538    CD1                                                 
REMARK 470     PHE A 539    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     ASN A 544    CG   OD1                                            
REMARK 470     LEU A 545    CG   CD1  CD2                                       
REMARK 470     GLU A 549    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 550    CG   CD   CE   NZ                                   
REMARK 470     ILE A 552    CD1                                                 
REMARK 470     ILE A 554    CD1                                                 
REMARK 470     THR A 557    OG1  CG2                                            
REMARK 470     GLU A 558    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 562    CG1  CG2  CD1                                       
REMARK 470     ILE A 583    CD1                                                 
REMARK 470     ASP A 596    CG   OD1  OD2                                       
REMARK 470     ILE A 598    CG1  CG2  CD1                                       
REMARK 470     TYR A 616    CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 470     ASP A 617    CG   OD1  OD2                                       
REMARK 470     ILE A 625    CD1                                                 
REMARK 470     GLU A 629    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 648    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 651    CD   CE   NZ                                        
REMARK 470     ILE A 652    CD1                                                 
REMARK 470     ARG A 656    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 660    CD1                                                 
REMARK 470     ILE A 698    CD1                                                 
REMARK 470     SER A 707    OG                                                  
REMARK 470     LYS A 708    CG   CD   CE   NZ                                   
REMARK 470     ASP A 709    CG   OD1  OD2                                       
REMARK 470     LYS A 710    CG   CD   CE   NZ                                   
REMARK 470     LYS A 711    CG   CD   CE   NZ                                   
REMARK 470     ILE A 716    CD1                                                 
REMARK 470     MET A 726    SD   CE                                             
REMARK 470     LEU A 750    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A 693   CB    CYS A 693   SG     -0.125                       
REMARK 500    CYS A 730   CB    CYS A 730   SG     -0.099                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 288   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  48      142.57    -37.17                                   
REMARK 500    TYR A  59      -61.20   -138.46                                   
REMARK 500    PRO A  69      176.27    -53.22                                   
REMARK 500    ASN A 209      177.49     95.56                                   
REMARK 500    ARG A 269      -21.66     92.08                                   
REMARK 500    LEU A 286      137.86    -37.20                                   
REMARK 500    ILE A 312       32.64    -80.56                                   
REMARK 500    GLU A 449      -55.72     77.32                                   
REMARK 500    ASN A 459     -127.99     63.42                                   
REMARK 500    LYS A 485      -58.37     75.36                                   
REMARK 500    GLN A 519      -65.86   -128.78                                   
REMARK 500    ASN A 531     -154.10    -74.58                                   
REMARK 500    GLU A 579     -125.05     48.98                                   
REMARK 500    CYS A 693      163.17    -48.61                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 751                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3LN7   RELATED DB: PDB                                   
DBREF  3LN6 A    1   750  UNP    Q8DXM9   GSHAB_STRA5      1    750             
SEQRES   1 A  750  MET ILE ILE ASP ARG LEU LEU GLN ARG SER HIS SER HIS          
SEQRES   2 A  750  LEU PRO ILE LEU GLN ALA THR PHE GLY LEU GLU ARG GLU          
SEQRES   3 A  750  SER LEU ARG ILE HIS GLN PRO THR GLN ARG VAL ALA GLN          
SEQRES   4 A  750  THR PRO HIS PRO LYS THR LEU GLY SER ARG ASN TYR HIS          
SEQRES   5 A  750  PRO TYR ILE GLN THR ASP TYR SER GLU PRO GLN LEU GLU          
SEQRES   6 A  750  LEU ILE THR PRO ILE ALA LYS ASP SER GLN GLU ALA ILE          
SEQRES   7 A  750  ARG PHE LEU LYS ALA ILE SER ASP VAL ALA GLY ARG SER          
SEQRES   8 A  750  ILE ASN HIS ASP GLU TYR LEU TRP PRO LEU SER MET PRO          
SEQRES   9 A  750  PRO LYS VAL ARG GLU GLU ASP ILE GLN ILE ALA GLN LEU          
SEQRES  10 A  750  GLU ASP ALA PHE GLU TYR ASP TYR ARG LYS TYR LEU GLU          
SEQRES  11 A  750  LYS THR TYR GLY LYS LEU ILE GLN SER ILE SER GLY ILE          
SEQRES  12 A  750  HIS TYR ASN LEU GLY LEU GLY GLN GLU LEU LEU THR SER          
SEQRES  13 A  750  LEU PHE GLU LEU SER GLN ALA ASP ASN ALA ILE ASP PHE          
SEQRES  14 A  750  GLN ASN GLN LEU TYR MET LYS LEU SER GLN ASN PHE LEU          
SEQRES  15 A  750  ARG TYR ARG TRP LEU LEU THR TYR LEU TYR GLY ALA SER          
SEQRES  16 A  750  PRO VAL ALA GLU GLU ASP PHE LEU ASP GLN LYS LEU ASN          
SEQRES  17 A  750  ASN PRO VAL ARG SER LEU ARG ASN SER HIS LEU GLY TYR          
SEQRES  18 A  750  VAL ASN HIS LYS ASP ILE ARG ILE SER TYR THR SER LEU          
SEQRES  19 A  750  LYS ASP TYR VAL ASN ASP LEU GLU ASN ALA VAL LYS SER          
SEQRES  20 A  750  GLY GLN LEU ILE ALA GLU LYS GLU PHE TYR SER PRO VAL          
SEQRES  21 A  750  ARG LEU ARG GLY SER LYS ALA CYS ARG ASN TYR LEU GLU          
SEQRES  22 A  750  LYS GLY ILE THR TYR LEU GLU PHE ARG THR PHE ASP LEU          
SEQRES  23 A  750  ASN PRO PHE SER PRO ILE GLY ILE THR GLN GLU THR VAL          
SEQRES  24 A  750  ASP THR VAL HIS LEU PHE LEU LEU ALA LEU LEU TRP ILE          
SEQRES  25 A  750  ASP SER SER SER HIS ILE ASP GLN ASP ILE LYS GLU ALA          
SEQRES  26 A  750  ASN ARG LEU ASN ASP LEU ILE ALA LEU SER HIS PRO LEU          
SEQRES  27 A  750  GLU LYS LEU PRO ASN GLN ALA PRO VAL SER ASP LEU VAL          
SEQRES  28 A  750  ASP ALA MET GLN SER VAL ILE GLN HIS PHE ASN LEU SER          
SEQRES  29 A  750  PRO TYR TYR GLN ASP LEU LEU GLU SER VAL LYS ARG GLN          
SEQRES  30 A  750  ILE GLN SER PRO GLU LEU THR VAL ALA GLY GLN LEU LEU          
SEQRES  31 A  750  GLU MET ILE GLU GLY LEU SER LEU GLU THR PHE GLY GLN          
SEQRES  32 A  750  ARG GLN GLY GLN ILE TYR HIS ASP TYR ALA TRP GLU ALA          
SEQRES  33 A  750  PRO TYR ALA LEU LYS GLY TYR GLU THR MET GLU LEU SER          
SEQRES  34 A  750  THR GLN LEU LEU LEU PHE ASP VAL ILE GLN LYS GLY VAL          
SEQRES  35 A  750  ASN PHE GLU VAL LEU ASP GLU GLN ASP GLN PHE LEU LYS          
SEQRES  36 A  750  LEU TRP HIS ASN SER HIS ILE GLU TYR VAL LYS ASN GLY          
SEQRES  37 A  750  ASN MET THR SER LYS ASP ASN TYR ILE VAL PRO LEU ALA          
SEQRES  38 A  750  MET ALA ASN LYS VAL VAL THR LYS LYS ILE LEU ASP GLU          
SEQRES  39 A  750  LYS HIS PHE PRO THR PRO PHE GLY ASP GLU PHE THR ASP          
SEQRES  40 A  750  ARG LYS GLU ALA LEU ASN TYR PHE SER GLN ILE GLN ASP          
SEQRES  41 A  750  LYS PRO ILE VAL VAL LYS PRO LYS SER THR ASN PHE GLY          
SEQRES  42 A  750  LEU GLY ILE SER ILE PHE LYS THR SER ALA ASN LEU ALA          
SEQRES  43 A  750  SER TYR GLU LYS ALA ILE ASP ILE ALA PHE THR GLU ASP          
SEQRES  44 A  750  SER ALA ILE LEU VAL GLU GLU TYR ILE GLU GLY THR GLU          
SEQRES  45 A  750  TYR ARG PHE PHE VAL LEU GLU GLY ASP CYS ILE ALA VAL          
SEQRES  46 A  750  LEU LEU ARG VAL ALA ALA ASN VAL VAL GLY ASP GLY ILE          
SEQRES  47 A  750  HIS THR ILE SER GLN LEU VAL LYS LEU LYS ASN GLN ASN          
SEQRES  48 A  750  PRO LEU ARG GLY TYR ASP HIS ARG SER PRO LEU GLU VAL          
SEQRES  49 A  750  ILE GLU LEU GLY GLU VAL GLU GLN LEU MET LEU GLU GLN          
SEQRES  50 A  750  GLN GLY TYR THR VAL ASN SER ILE PRO PRO GLU GLY THR          
SEQRES  51 A  750  LYS ILE GLU LEU ARG ARG ASN SER ASN ILE SER THR GLY          
SEQRES  52 A  750  GLY ASP SER ILE ASP VAL THR ASN THR MET ASP PRO THR          
SEQRES  53 A  750  TYR LYS GLN LEU ALA ALA GLU MET ALA GLU ALA MET GLY          
SEQRES  54 A  750  ALA TRP VAL CYS GLY VAL ASP LEU ILE ILE PRO ASN ALA          
SEQRES  55 A  750  THR GLN ALA TYR SER LYS ASP LYS LYS ASN ALA THR CYS          
SEQRES  56 A  750  ILE GLU LEU ASN PHE ASN PRO LEU MET TYR MET HIS THR          
SEQRES  57 A  750  TYR CYS GLN GLU GLY PRO GLY GLN SER ILE THR PRO ARG          
SEQRES  58 A  750  ILE LEU ALA LYS LEU PHE PRO GLU LEU                          
HET    SO4  A 751       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3  HOH   *35(H2 O)                                                     
HELIX    1   1 LEU A    6  SER A   10  5                                   5    
HELIX    2   2 ASP A   73  ILE A   92  1                                  20    
HELIX    3   3 ASP A  119  GLY A  134  1                                  16    
HELIX    4   4 LYS A  135  ILE A  140  5                                   6    
HELIX    5   5 GLY A  150  GLN A  162  1                                  13    
HELIX    6   6 ASN A  165  TYR A  192  1                                  28    
HELIX    7   7 SER A  233  ALA A  244  1                                  12    
HELIX    8   8 ALA A  252  PHE A  256  5                                   5    
HELIX    9   9 THR A  295  ILE A  312  1                                  18    
HELIX   10  10 HIS A  317  SER A  335  1                                  19    
HELIX   11  11 PRO A  346  ASN A  362  1                                  17    
HELIX   12  12 SER A  364  SER A  380  1                                  17    
HELIX   13  13 PRO A  381  LEU A  383  5                                   3    
HELIX   14  14 THR A  384  ILE A  393  1                                  10    
HELIX   15  15 LEU A  398  TRP A  414  1                                  17    
HELIX   16  16 LEU A  420  GLU A  424  5                                   5    
HELIX   17  17 GLU A  427  GLY A  441  1                                  15    
HELIX   18  18 TYR A  476  MET A  482  1                                   7    
HELIX   19  19 LYS A  485  LYS A  495  1                                  11    
HELIX   20  20 GLU A  510  ILE A  518  1                                   9    
HELIX   21  21 ASN A  544  ASP A  559  1                                  16    
HELIX   22  22 THR A  600  ASN A  609  1                                  10    
HELIX   23  23 GLY A  628  GLN A  638  1                                  11    
HELIX   24  24 ASP A  674  MET A  688  1                                  15    
HELIX   25  25 MET A  724  TYR A  729  1                                   6    
HELIX   26  26 ILE A  738  PHE A  747  1                                  10    
SHEET    1   A 3 ARG A  36  VAL A  37  0                                        
SHEET    2   A 3 ALA A  19  HIS A  31 -1  N  HIS A  31   O  ARG A  36           
SHEET    3   A 3 GLU A  96  LEU A  98 -1  O  TYR A  97   N  ILE A  30           
SHEET    1   B 6 ILE A  55  THR A  57  0                                        
SHEET    2   B 6 GLN A  63  ILE A  67 -1  O  GLU A  65   N  GLN A  56           
SHEET    3   B 6 ALA A  19  HIS A  31 -1  N  SER A  27   O  LEU A  64           
SHEET    4   B 6 ILE A 143  LEU A 149 -1  O  GLY A 148   N  THR A  20           
SHEET    5   B 6 TYR A 278  PHE A 281 -1  O  PHE A 281   N  TYR A 145           
SHEET    6   B 6 VAL A 260  ARG A 263 -1  N  ARG A 261   O  GLU A 280           
SHEET    1   C 3 ASN A 443  VAL A 446  0                                        
SHEET    2   C 3 PHE A 453  HIS A 458 -1  O  LYS A 455   N  GLU A 445           
SHEET    3   C 3 HIS A 461  LYS A 466 -1  O  GLU A 463   N  LEU A 456           
SHEET    1   D 4 PHE A 505  THR A 506  0                                        
SHEET    2   D 4 ALA A 561  GLU A 566 -1  O  ILE A 562   N  PHE A 505           
SHEET    3   D 4 ILE A 523  PRO A 527 -1  N  LYS A 526   O  LEU A 563           
SHEET    4   D 4 SER A 537  PHE A 539 -1  O  SER A 537   N  VAL A 525           
SHEET    1   E 5 ASP A 665  ASP A 668  0                                        
SHEET    2   E 5 ASP A 581  VAL A 589 -1  N  LEU A 587   O  ILE A 667           
SHEET    3   E 5 THR A 571  LEU A 578 -1  N  ARG A 574   O  LEU A 586           
SHEET    4   E 5 GLY A 694  ILE A 699 -1  O  VAL A 695   N  PHE A 575           
SHEET    5   E 5 THR A 714  ASN A 719 -1  O  ASN A 719   N  GLY A 694           
SHEET    1   F 2 ASN A 592  VAL A 594  0                                        
SHEET    2   F 2 LYS A 651  GLU A 653 -1  O  ILE A 652   N  VAL A 593           
SHEET    1   G 2 ARG A 614  GLY A 615  0                                        
SHEET    2   G 2 LEU A 622  GLU A 623  1  O  LEU A 622   N  GLY A 615           
SITE     1 AC1  5 ARG A 588  ASN A 659  ILE A 660  SER A 661                    
SITE     2 AC1  5 HOH A 776                                                     
CRYST1  143.020  143.020  211.230  90.00  90.00  90.00 I 41 2 2     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006992  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006992  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004734        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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